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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Ubiquitin carboxyl-terminal hydrolase L5

Top mentioned proteins: Ubiquitin, CAN, Adrm1, Ubiquitin Thiolesterase, USP14
Papers on UCH37
A new ER-specific photosensitizer unravels (1)O2-driven protein oxidation and inhibition of deubiquitinases as a generic mechanism for cancer PDT.
Feron et al., Brussels, Belgium. In Oncogene, Jan 2016
This new class of PS unraveled an unsuspected common mechanism of action for PS that involves the combined inhibition of the mammalian target of rapamycin (mTOR) signaling pathway and proteasomal deubiquitinases (DUBs) USP14 and UCH37.
Naturally Occurring Isothiocyanates Exert Anticancer Effects by Inhibiting Deubiquitinating Enzymes.
Hedstrom et al., Amsterdam, Netherlands. In Cancer Res, Jan 2016
Here we report that BITC and PEITC effectively inhibit deubiquitinating enzymes (DUB), including the enzymes USP9x and UCH37, which are associated with tumorigenesis, at physiologically relevant concentrations and time scales.
Regulation of E2 Promoter Binding Factor 1 (E2F1) Transcriptional Activity through a Deubiquitinating Enzyme, UCH37.
Lin et al., Houston, United States. In J Biol Chem, Nov 2015
Here we identify UCH37 as the first, to our knowledge, deubiquitinating enzyme for E2F1.
Structural plasticity allows UCH37 to be primed by RPN13 or locked down by INO80G.
Walters et al., Frederick, United States. In Mol Cell, Apr 2015
(2015),report crystal structures that define how deubiquitinating enzyme UCH37 is switched on or off by proteasome ubiquitin receptor RPN13 or chromatin remodeler component INO80G.
Ubiquitination and regulation of Smad7 in the TGF-β1/Smad signaling of aristolochic acid nephropathy.
Wu et al., Beijing, China. In Toxicol Mech Methods, 2014
We aimed to clarify whether Arkadia and UCH37 participate in TGF-β1/Smad signaling via Smad7, and the regulatory mechanisms of Smad7.
A High Affinity hRpn2-Derived Peptide That Displaces Human Rpn13 from Proteasome in 293T Cells.
Walters et al., Frederick, United States. In Plos One, 2014
Its ubiquitin-binding activity is confined to an N-terminal Pru (pleckstrin-like receptor for ubiquitin) domain that also docks it into the proteasome, while its C-terminal DEUBAD (DEUBiquitinase ADaptor) domain recruits deubiquitinating enzyme Uch37 to the proteasome.
Activity-Based Proteomic Profiling of Deubiquitinating Enzymes in Salmonella-Infected Macrophages Leads to Identification of Putative Function of UCH-L5 in Inflammasome Regulation.
Edelmann et al., United States. In Plos One, 2014
Also, we detected down-regulation of UCH-L3, and USP4 as well as up-regulation of USP5 and UCH-L5 deubiquitinating enzymes in macrophages infected with Salmonella Typhimurium.
Power and promise of ubiquitin carboxyl-terminal hydrolase 37 as a target of cancer therapy.
Shen et al., Shanghai, China. In Asian Pac J Cancer Prev, 2012
Ubiquitin carboxyl-terminal hydrolase 37 (UCH37, also called UCHL5), a member of the deubiquitinating enzymes, can suppress protein degradation through disassembling polyubiquitin from the distal subunit of the chain.
Expression and clinical significance of UCH37 in human esophageal squamous cell carcinoma.
Shen et al., Shanghai, China. In Dig Dis Sci, 2012
UCH37 is associated with outcome and recurrence of ESCC and can be a novel predictor for poor prognosis of esophageal squamous cell carcinoma patients after curative resection.
The interaction between ubiquitin C-terminal hydrolase 37 and glucose-regulated protein 78 in hepatocellular carcinoma.
Shen et al., Shanghai, China. In Mol Cell Biochem, 2012
a functional proteomic analysis was performed to screen UCH37-interacting proteins in hepatocellular carcinoma (HCC), and glucose-regulated protein 78 was identified as one interacting with UCH37
Crystal structure of the catalytic domain of UCHL5, a proteasome-associated human deubiquitinating enzyme, reveals an unproductive form of the enzyme.
Das et al., West Lafayette, United States. In Febs J, 2011
our structures reveal conformationally dynamic parts of the enzyme that may play a role in the structural transition to the more active form.
Trimming of ubiquitin chains by proteasome-associated deubiquitinating enzymes.
Finley et al., Boston, United States. In Mol Cell Proteomics, 2011
Substrate deubiquitination on the proteasome is mediated by three distinct deubiquitinating enzymes associated with the regulatory particle: RPN11, UCH37, and USP14.
Effect of ubiquitin carboxy-terminal hydrolase 37 on apoptotic in A549 cells.
Chen et al., Shanghai, China. In Cell Biochem Funct, 2011
Silencing of UCH37 in A549 cells induced apoptosis.
The potential role of ubiquitin c-terminal hydrolases in oncogenesis.
Shen et al., Shanghai, China. In Biochim Biophys Acta, 2010
The ubiquitin C-terminal hydrolases (UCHs) subfamily of DUBs consists of four members: UCH-L1, UCH-L3, UCH37 and BRCA1-associated protein-1 (BAP1).
Effects of ethanol on the proteasome interacting proteins.
Bardag-Gorce, Los Angeles, United States. In World J Gastroenterol, 2010
Interaction of the proteasome with Ecm29 and with deubiquitinating enzymes Rpn11, UCH37, and Usp14 has been found to decrease.
Regulators of the proteasome pathway, Uch37 and Rpn13, play distinct roles in mouse development.
Oravecz et al., The Woodlands, United States. In Plos One, 2009
this is the first report characterizing the physiological roles of Uch37 and Rpn13 in murine development and implicating a non-ATPase proteasomal protein, Rpn13, in the process of gametogenesis
Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interaction.
Groll et al., Garching bei München, Germany. In Nature, 2008
In the accompanying manuscript we report that Rpn13 (refs 3-7), a component of the nine-subunit proteasome base, functions as a ubiquitin receptor, complementing its known role in docking de-ubiquitinating enzyme Uch37/UCHL5 (refs 4-6) to the proteasome.
Proteasome subunit Rpn13 is a novel ubiquitin receptor.
Dikic et al., Frankfurt am Main, Germany. In Nature, 2008
Because Rpn13 is also the proteasomal receptor for Uch37, a deubiquitinating enzyme, our findings suggest a coupling of chain recognition and disassembly at the proteasome.
New insights into the role of the ubiquitin-proteasome pathway in the regulation of apoptosis.
Qiu et al., Beijing, China. In Chang Gung Med J, 2007
In this review, we attempt to highlight the recent progress in research on UPP and its role in the regulation of apoptosis by focusing on several of its important components, including the ubiqutin ligase Nrdp 1, which regulates ErbB/EGFR family of receptor tyrosine kinases, the ubiquitin-carrier protein BRUCE/Apollon (an Inhibitor of Apoptosis Protein), and the novel proteasome subunit hRpnl3 (a binding site for the deubiquitinating enzyme, UCH37).
Proteasome recruitment and activation of the Uch37 deubiquitinating enzyme by Adrm1.
Cohen et al., Kansas City, United States. In Nat Cell Biol, 2006
Neither Uch37 alone nor the Uch37-Adrm1 or Uch37-Adrm1-S1 complexes can hydrolyse di-ubiquitin efficiently; rather, incorporation into the 19S complex is required to enable processing of polyubiquitin chains.
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